Her primary scientific interests are in Biochemistry, Dipeptidyl peptidase, Enzyme, Oligopeptidase and Stereochemistry. Her study brings together the fields of Molecular biology and Biochemistry. She interconnects Serine, Chemokine, Enzyme inhibitor, Peptide and Dipeptidyl peptidase-4 in the investigation of issues within Dipeptidyl peptidase.
Her work carried out in the field of Enzyme brings together such families of science as Ion chromatography, Adenosine and Prostasomes. Her Oligopeptidase research is multidisciplinary, incorporating perspectives in Serine protease, Dipeptidyl-peptidase II, Function, Viability assay and Fibroblast activation protein, alpha. Her study in Stereochemistry is interdisciplinary in nature, drawing from both Phosphonate, Reaction intermediate, Ferrous, Prostaglandin and ATP synthase.
Anne-Marie Lambeir mostly deals with Biochemistry, Dipeptidyl peptidase, Enzyme, Stereochemistry and Oligopeptidase. Biochemistry and Molecular biology are commonly linked in her work. Her research in Dipeptidyl peptidase intersects with topics in Serine, Endocrinology, Internal medicine and Dipeptidyl peptidase-4.
She has included themes like Biological activity and Dipeptidyl peptidase 8 in her Enzyme study. As a part of the same scientific family, she mostly works in the field of Stereochemistry, focusing on Isomerase and, on occasion, Active site. She combines subjects such as Serine protease, Fibroblast activation protein, alpha and Function with her study of Oligopeptidase.
Her primary areas of investigation include Cell biology, Oligopeptidase, Pharmacology, Biochemistry and Fibroblast activation protein, alpha. Her biological study spans a wide range of topics, including Arrhenius plot, Hemoglobin, Prolyl endopeptidase, Coefficient of variation and Dipeptidyl peptidase. Her Dipeptidyl peptidase research includes elements of Cancer, Oligopeptidase A, Ligand, Exopeptidase and Enzyme kinetics.
Her Pharmacology research is multidisciplinary, relying on both Proteases, Fibrinolysis, Serine and Carboxypeptidase B2. Her Biochemistry study integrates concerns from other disciplines, such as Porphyromonas gingivalis, Biophysics and Hydrogen–deuterium exchange. Her Fibroblast activation protein, alpha research includes themes of Serine protease, Fibroblast, Molecular biology and Platelet.
The scientist’s investigation covers issues in Cell biology, Fibroblast activation protein, alpha, Pharmacology, Protease and Immunology. Her work deals with themes such as Biomarker, Peripheral blood mononuclear cell, Cell junction and Intestinal permeability, which intersect with Cell biology. The Fibroblast activation protein, alpha study combines topics in areas such as Serine protease, Small molecule and Tissue remodeling.
Her Pharmacology study deals with Irritable bowel syndrome intersecting with Proteases. The concepts of her Protease study are interwoven with issues in Pyroptosis, Inflammasome, Cytokine, Apoptosis and Secretion. As part of the same scientific family, Anne-Marie Lambeir usually focuses on Immunology, concentrating on Dipeptidyl peptidase and intersecting with Oligopeptidase.
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Dipeptidyl-peptidase IV from bench to bedside: an update on structural properties, functions, and clinical aspects of the enzyme DPP IV.
Anne-Marie Lambeir;Christine Durinx;Simon Scharpé;Ingrid De Meester.
Critical Reviews in Clinical Laboratory Sciences (2003)
Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection.
Paul Proost;Ingrid De Meester;Dominique Schols;Sofie Struyf.
Journal of Biological Chemistry (1998)
Molecular characterization of dipeptidyl peptidase activity in serum: soluble CD26/dipeptidyl peptidase IV is responsible for the release of X-Pro dipeptides.
Christine Durinx;Anne-Marie Lambeir;Eugène Bosmans;Jean-Bernard Falmagne.
FEBS Journal (2000)
Kinetic Investigation of Chemokine Truncation by CD26/Dipeptidyl Peptidase IV Reveals a Striking Selectivity within the Chemokine Family
Anne-Marie Lambeir;Paul Proost;Christine Durinx;Gunther Bal.
Journal of Biological Chemistry (2001)
Amino-terminal truncation of CXCR3 agonists impairs receptor signaling and lymphocyte chemotaxis, while preserving antiangiogenic properties
Paul Proost;Evemie Schutyser;Patricia Menten;Sofie Struyf.
Blood (2001)
Dipeptidyl-peptidase IV converts intact B-type natriuretic peptide into its des-SerPro form.
Inger Brandt;Anne-Marie Lambeir;Jean-Marie Ketelslegers;Marc Vanderheyden.
Clinical Chemistry (2006)
Spectral properties of the higher oxidation states of prostaglandin H synthase.
Lambeir Am;Markey Cm;Dunford Hb;Marnett Lj.
Journal of Biological Chemistry (1985)
Truncation of Macrophage-derived Chemokine by CD26/ Dipeptidyl-Peptidase IV beyond Its Predicted Cleavage Site Affects Chemotactic Activity and CC Chemokine Receptor 4 Interaction
Paul Proost;Sofie Struyf;Dominique Schols;Ghislain Opdenakker.
Journal of Biological Chemistry (1999)
The unique properties of dipeptidyl-peptidase IV (DPP IV / CD26) and the therapeutic potential of DPP IV inhibitors.
K Augustyns;G Bal;G Thonus;A Belyaev.
Current Medicinal Chemistry (1999)
Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by Vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino]acetyl}-pyrrolidine-2-carbonitrile).
Inger Brandt;Jurgen Joossens;Xin Chen;Marie-Berthe Maes.
Biochemical Pharmacology (2005)
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